PROSITE documentation PDOC50950Zinc finger THAP-type profile
The THAP-type zinc finger (consensus: C-x(2,4)-C-x(35,50)-C-x(2)-H) is an ~90-residue domain restricted to animals, which is shared between the THAP family of cellular DNA-binding proteins, and transposases from mobile genomic parasites [1,2]. THAP1, the prototype of the THAP family, possesses zinc-dependent sequence-specific DNA binding activity and recognizes a consensus DNA target sequence of 11 nucleotides [3]. The THAP-type zinc finger can be found in one or more copies and can be associated with other domains, such as the C2H2-type zinc finger (see <PDOC00028>).
The structure of the THAP-type zinc finger (see <PDB:2JTG>) reveals the presence between the C2CH zinc coordinating residues of a short antiparallel β-sheet interspersed by a long loop-helix-loop insertion. This loop-helix-loop motif has been shown to be essential for the identification of a number of critical residues for DNA recognition [4].
Some proteins known to contain a THAP-type zinc finger are listed below:
- Mammalian Thanatos-associated protein-1 (THAP1). It potentiates both serum withdrawal- and tumor necrosis factor α-induced apoptosis, and interacts with prostate-apoptosis-response 4 (Par4), a well-characterized proapoptotic factor.
- Mammalian death-associated protein DAP4/p52rIPK or THAP0. It has been identified in a genetic screen for genes involved in interferon-γ- induced apoptosis in HeLa cells and in a two-hybrid screen for indirect activators of the interferon-induced kinase PKR, an important mediator of stress-induced apoptosis.
- Mammalian THAP2 to THAP11.
- Drosophila melanogaster dorsal interacting protein 2 (DIP2).
- Drosophila melanogaster P element transposase.
The profile we developed covers the whole THAP-type zinc finger with 4 positions upstream, and about 20 positions downstream.
Last update:September 2008 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Roussigne M. Kossida S. Lavigne A.-C. Clouaire T. Ecochard V. Glories A. Amalric F. Girard J.-P. |
| Title | The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase. | |
| Source | Trends Biochem. Sci. 28:66-69(2003). | |
| PubMed ID | 12575992 |
| 2 | Authors | Roussigne M. Cayrol C. Clouaire T. Amalric F. Girard J.-P. |
| Title | THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. | |
| Source | Oncogene 22:2432-2442(2003). | |
| PubMed ID | 12717420 | |
| DOI | 10.1038/sj.onc.1206271 |
| 3 | Authors | Clouaire T. Roussigne M. Ecochard V. Mathe C. Amalric F. Girard J.P. |
| Title | The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 102:6907-6912(2005). | |
| PubMed ID | 15863623 | |
| DOI | 10.1073/pnas.0406882102 |
| 4 | Authors | Bessiere D. Lacroix C. Campagne S. Ecochard V. Guillet V. Mourey L. Lopez F. Czaplicki J. Demange P. Milon A. Girard J.P. Gervais V. |
| Title | Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways. | |
| Source | J. Biol. Chem. 283:4352-4363(2008). | |
| PubMed ID | 18073205 | |
| DOI | 10.1074/jbc.M707537200 |
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